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Crystallization and X‐ray analysis of a single fab binding domain from protein L of Peptostreptococcus magnus
Author(s) -
Sohi Maninder K.,
Wan Tommy,
Sutton Brian J.,
Atkinson Tony,
Atkinson Max A.,
Murphy Jonathan P.,
Bottomley Stephen P.,
Gore Michael G.
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340230420
Subject(s) - crystallography , chemistry , immunoglobulin domain , crystallization , diffraction , molecule , domain (mathematical analysis) , resolution (logic) , x ray crystallography , stereochemistry , physics , optics , receptor , mathematics , biochemistry , mathematical analysis , organic chemistry , artificial intelligence , computer science
Protein L is a multi domain cell wall constituent of certain strains of Peptostreptococcus magnus which binds to the variable domain of immunoglobulin κ‐light chains. A single immunoglobulin‐binding domain of M r = 9000 from this protein has been isolated and crystallized. The crystals are of space group P 4 2 2 1 2, with cell dimensions a = b = 66.9 Å, c = 68.3 Å, and diffract to at least 2.2 Å resolution. The asymmetric unit of the crystal contains two molecules of the protein L domain, related by a noncrystallographic 2‐fold axis, as revealed by a self‐rotation function calculated with native diffraction data. © 1995 Wiley‐Liss, Inc.